Abnormal accumulation of alpha-synuclein (SYN) in the nervous system results in progressive damage to neurons leading to Parkinson's Disease (PD). The SYN molecule also has been shown to aggregate and promote nerve cell damage in other neurological disorders including Alzheimer's Disease (AD), Lewy body disease (LBD) and Multiple system atrophy (MSA). SYN is a 140 amino acid (aa) nerve terminal molecule involved in synaptic plasticity and dopamine release.
Proteins and peptides that function as chaperone molecules or that have some homology with SYN (e.g.: HSP-70 and beta-synuclein) and small compounds (e.g.: Rifampicin and flavinoids) have been described to block SYN aggregation and fibrillation.